MVD2_PANGI
ID MVD2_PANGI Reviewed; 420 AA.
AC F8QQQ7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Diphosphomevalonate decarboxylase 2 {ECO:0000305};
DE Short=Mevalonate-5-pyrophosphate decarboxylase {ECO:0000303|PubMed:24933610};
DE Short=PgMVD {ECO:0000303|PubMed:24933610};
DE EC=4.1.1.33 {ECO:0000250|UniProtKB:O23722};
GN Name=MVD2 {ECO:0000305};
GN Synonyms=MPD {ECO:0000303|PubMed:29509695},
GN MVD {ECO:0000303|PubMed:24933610};
OS Panax ginseng (Korean ginseng).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Panax.
OX NCBI_TaxID=4054;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=24933610; DOI=10.1021/sb400194g;
RA Kim Y.-K., Kim Y.B., Uddin M.R., Lee S., Kim S.-U., Park S.U.;
RT "Enhanced triterpene accumulation in Panax ginseng hairy roots
RT overexpressing mevalonate-5-pyrophosphate decarboxylase and farnesyl
RT pyrophosphate synthase.";
RL ACS Synth. Biol. 3:773-779(2014).
RN [2]
RP REVIEW.
RX PubMed=29378087; DOI=10.1002/bab.1649;
RA Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.;
RT "Advances in ginsenoside biosynthesis and metabolic regulation.";
RL Biotechnol. Appl. Biochem. 65:514-522(2018).
RN [3]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=29509695; DOI=10.3390/molecules23030589;
RA Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.;
RT "Progress on the studies of the key enzymes of ginsenoside biosynthesis.";
RL Molecules 23:0-0(2018).
CC -!- FUNCTION: Performs the first committed step in the biosynthesis of
CC isoprene-containing compounds such as sterols and terpenoids (By
CC similarity). Component of the triterpenes (e.g. ginsenosides or
CC panaxosides) and phytosterols biosynthetic pathways (PubMed:24933610,
CC PubMed:29378087). Promotes the accumulation of stigmasterol and beta-
CC sitosterol (PubMed:24933610). {ECO:0000250|UniProtKB:O23722,
CC ECO:0000269|PubMed:24933610, ECO:0000303|PubMed:29378087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl
CC diphosphate + phosphate; Xref=Rhea:RHEA:23732, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57557,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=4.1.1.33;
CC Evidence={ECO:0000250|UniProtKB:O23722};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 3/3. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O23722}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O23722}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; GU565096; ADI80345.1; -; mRNA.
DR AlphaFoldDB; F8QQQ7; -.
DR SMR; F8QQQ7; -.
DR BRENDA; 4.1.1.33; 7895.
DR UniPathway; UPA00057; UER00100.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016135; P:saponin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR005935; Mev_decarb.
DR InterPro; IPR029765; Mev_diP_decarb.
DR InterPro; IPR041431; Mvd1_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF18376; MDD_C; 1.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR01240; mevDPdecarb; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Nucleotide-binding; Peroxisome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..420
FT /note="Diphosphomevalonate decarboxylase 2"
FT /id="PRO_0000446950"
FT MOTIF 42..50
FT /note="Peroxisomal targeting signal PTS2"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 25..28
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 80
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 163..168
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 219
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
SQ SEQUENCE 420 AA; 46590 MW; 7816E898E353EFD1 CRC64;
MAKELQKWVV MVTAQTPTNI AVIKYWGKRD ETLILPINDS ISVTLDPDHL CTTTTVSVSP
SFEQDRMWLN GKEISLLGGR FQSCLREIRS RACDLEDEKK GIKIKKMDWE KLRLHIASYN
NFPTAAGLAS SAAGLACFVF ALAKLMNLNE DNGQLSAIAR RGSGSACRSL YGGFVKWIMG
KEENGSDSIA FQLADEKHWD DLVIVIAVVS ARQKETSSTT GMQDSCKTSM LIQHRAKEVV
PKRIIQMEDA IEKRDFPSFA RLACADSNQF HAVCLDTSPP IFYMNDTSHK IISCVEKWNR
SVGTPQVAYT FDAGPNAVLI ARDRKIAALL LRRLLFHFPP TFQHCLNSYV IGDKSILQDV
GVQDMKDIES LPPPPEIKDN IPAQKSNGDV SYFICTRPGR GPVLLPDSGA LLNPETGLPK
